Studies on the interaction of the dye, stains-all, with individual calcium-binding domains of calmodulin.

Abstract:

:We show that the calcium-mimic dye, Stains-all, is a convenient probe to study the structural features of the individual calcium-binding sites of calmodulin (CaM) and related calcium-binding proteins (CaBP). These peptides bind the dye in their calcium-binding sites, and induce a circular dichroism (CD) band in the bound dye in the 620 nm (J band) region, which is abolished upon the addition of calcium. Replacement of Asp by Asn in the + x position of the weaker calcium-binding site (site I of CaM) abolishes the dye binding, while the same change in the higher affinity site IV attenuates the binding of the dye and does not abolish it. Replacement of Tyr in site IV with Trp does not distort the geometry, although it increases the dye binding affinity.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Sharma Y,Gopalakrishna A,Balasubramanian D,Fairwell T,Krishna G

doi

10.1016/0014-5793(93)81761-n

subject

Has Abstract

pub_date

1993-07-12 00:00:00

pages

59-64

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(93)81761-N

journal_volume

326

pub_type

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